Lipid chain-driven interaction of a lipidated Src-family kinase Lyn with the bilayer membrane.

-Myristoylation is a process of ubiquitous protein modification, which promotes the interaction of lipidated proteins on cell surfaces, in conjunction with reversible -palmitoylation. We report the cooperative lipid-lipid interaction of two acyl chains of proteins, which increases the protein-membrane interaction and facilitates selective targeting of membranes containing anionic lipids. Lyn is a member of the Src family kinases distributed on the membrane surface by -myristoyl and neighbouring -palmitoyl chain anchors at the unique N-terminus domain.